GCW_00095







Uniprot: A0A0F6CJS6
Description: ribonuclease J
EC number: 3.1.-.-
Annotation score: 2 out of 5
Miscellaneous [CC]: 
Protein existence: Inferred from homology
Catalytic activity: 
Cofactor: COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-Rule:MF_01491}; ; Note=Binds up to 2 Zn(2+) ions per subunit. It is not clear if Zn(2+) or Mg(2+) is physiologically important. {ECO:0000256|HAMAP-Rule:MF_01491}
Enzyme regulation: 
Function [CC]: FUNCTION: An RNase that has 5'-3' exonuclease and possibly endonuclease activity. Involved in maturation of rRNA and in some organisms also mRNA maturation and/or decay. {ECO:0000256|HAMAP-Rule:MF_01491}.
Pathway: 
Active site: 
Binding site: 
Calcium binding: 
DNA binding: 
Metal binding: METAL 80 80 Zinc 1; via tele nitrogen; catalytic. {ECO:0000256|HAMAP-Rule:MF_01491}.; METAL 82 82 Zinc 1; via pros nitrogen; catalytic. {ECO:0000256|HAMAP-Rule:MF_01491}.; METAL 84 84 Zinc 2; catalytic. {ECO:0000256|HAMAP-Rule:MF_01491}.; METAL 85 85 Zinc 2; via tele nitrogen; catalytic. {ECO:0000256|HAMAP-Rule:MF_01491}.; METAL 149 149 Zinc 1; via tele nitrogen; catalytic. {ECO:0000256|HAMAP-Rule:MF_01491}.; METAL 171 171 Zinc 1; catalytic. {ECO:0000256|HAMAP-Rule:MF_01491}.; METAL 171 171 Zinc 2; catalytic. {ECO:0000256|HAMAP-Rule:MF_01491}.; METAL 399 399 Zinc 2; via tele nitrogen; catalytic. {ECO:0000256|HAMAP-Rule:MF_01491}.
Nucleotide binding: 
Site: 
Gene names (primary): rnj
Gene names (synonym): 
Mass: 64,349
Subunit structure [CC]: SUBUNIT: Homodimer, may be a subunit of the RNA degradosome. {ECO:0000256|HAMAP-Rule:MF_01491}.
Gene ontology (GO): cytoplasm [GO:0005737]; 5'-3' exoribonuclease activity [GO:0004534]; endoribonuclease activity [GO:0004521]; RNA binding [GO:0003723]; zinc ion binding [GO:0008270]; rRNA processing [GO:0006364]
Gene ontology IDs: GO:0003723; GO:0004521; GO:0004534; GO:0005737; GO:0006364; GO:0008270
Chain: 
Signal peptide: 
Domain [CC]: 
Sequence similarities: SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-metabolizing metallo-beta-lactamase-like family. Bacterial RNase J subfamily. {ECO:0000256|HAMAP-Rule:MF_01491}.
Protein families: Metallo-beta-lactamase superfamily, RNA-metabolizing metallo-beta-lactamase-like family, Bacterial RNase J subfamily
Coiled coil: 
Domain [FT]: DOMAIN 27 222 Lactamase_B. {ECO:0000259|SMART:SM00849}.
Motif: 
Region: REGION 373 377 Substrate binding. {ECO:0000256|HAMAP-Rule:MF_01491, ECO:0000256|PIRSR:PIRSR004803-2}.
EMBL: CP006916
ProteinModelPortal: 
MEROPS: 
EnsemblBacteria KO: AHB99348
UniPathway: K12574
CDD: 
Gene3D: 
HAMAP: 3.60.15.10
InterPro: MF_01491
PANTHER: IPR001279;IPR011108;IPR004613;IPR030854
PIRSF: PTHR11203:SF22
PRINTS: PIRSF004803
PROSITE: 
Pfam: 
ProDom: PF00753;PF07521
SMART: 
SUPFAM: SM00849
TIGRFAMs: SSF56281
22106-23807(-)

>nucleotide sequence
TTAGATCTCTCTGATGTTTGATACCACCAGTGGGTTGCGGTGTTTGTTTCTCCAGATGTA
GAAACGGCAACTTTCGTGGATAATTTTCTTTAATTCGTGCTCTGAGTAGTTTTGGTTTTT
AGCTAAATACTCATTAGCATTAGTTTTAATCTCATAAGCAATCTTGGTCATTAGACCATG
ACTTTCTTTGAGATAGAAACAACCACTAGATTTTAGTTTAGGTAAAGTTTTAATCTGTTT
GCTTGCTTTATCAATTACGACAGTAATTGCAAAGATCCCCTCTTCAGATAACACCTGTCT
AGTGTTCATAATTCTTTTAACGTTAGGTGAAACTGATTTACCTTCGATGAAGAGTGGTTC
AGCATCGATCGTTTCTTTTGTGTAATACAGTTCACGATCGATTAGATAAACGATCTGACC
GTTTTTATGTAGGGCTACGTTTTCTGGGTCAAAACCACACTTTTTAGCAATTCTTTTTAA
AGAAGTAAACATCTTATATTCCCCATGGATTGGGAATAAGTATTTAGGTCTTAGCAAGCT
TAACATTAGTTGAATCTCTTGCATCGTTGCGTGACCAGAAGCGTGCAACTTTAACGTCGG
AGAATTTTCATAAATCGAGATCCCCTCTTCTTTAGATAGTTCGTTAAGTAGCCGTTCTAC
GGCTGCATAATTCCCCGGAATCGGGTTAGATGACATGATAATTGAATCGGTCTTTTTAAG
TTGGATCCAAGGATGACGCCCGCTTGCTAACATATTAAGTGCAGCCAACTCTTCTCCTTG
AGAACCCGTACAAAAGATCATGATCTCATTATCAGGGTGTTGTTCTACATATCTAGATTC
AACAATATCATCATCTTTAAGGTTAATATACCCAACATCTCGAGAGATCGAAACGTTATT
ATCCATCGATTTACCCAATAAACAGATCTTACGACCGTGTTGGATTGCGATCTCGATTAC
TTCACTTATTCTGGTAACGTTTGAAGCAAACGTTGATAAGATCACCCGTCCATTAGCATT
CTTGATAATATTTTTAATATTATCGTAGATCTCTTTTTCAGAGCTTGAAAACCCCGGGAT
CTCAGCATTCGTGGTTTCAGTCATAAACAGATCAATCCCACGTCTACTGATCTCAACGAC
TTTATGAATATCTAACTCTTCATTACCAGCATTAAAATCAAAACGGTAATCACCACTTTC
AACGATATTACCATTTGGTGTTTGAACACAAACACCAAATGCATCTGGGATCGAGTGACA
CACTCGATAAAAATCAATTTTAAAGTGTTTGGTACTAAACTCAGATTTATCGTTATATGA
AACGATCTTATATTGGTTTAGGTTATGGTGTTCATGTAATTTTTTCTCGATTAATTTAGT
TGCCATCAACGGCGCATAAATTACAGGAACACTAACCTCTCTTAATAAATAAGGAATTCC
CCCGATGTGGTCTTCATGACCATGGGTAATAACTAATGCCTTAATCTTGTGTTGGTTTGC
TTTTGCATAAGCAAAATTGGGAACGATCCCATCGATTCCTAATAGTTCAACAGAAGAGAA
CTTGATACCACAATCAACGATGATTAATTCATCGTCGTATTCGATACCATACATGTTTTT
TCCTACTTCTTCAAGTCCACCAAAAGCAAAGATTTTGGTGGGTTTTTTATTAGGATTAAT
ATCTTTAAAATCCTTAATCAT


>protein sequence
MIKDFKDINPNKKPTKIFAFGGLEEVGKNMYGIEYDDELIIVDCGIKFSSVELLGIDGIV
PNFAYAKANQHKIKALVITHGHEDHIGGIPYLLREVSVPVIYAPLMATKLIEKKLHEHHN
LNQYKIVSYNDKSEFSTKHFKIDFYRVCHSIPDAFGVCVQTPNGNIVESGDYRFDFNAGN
EELDIHKVVEISRRGIDLFMTETTNAEIPGFSSSEKEIYDNIKNIIKNANGRVILSTFAS
NVTRISEVIEIAIQHGRKICLLGKSMDNNVSISRDVGYINLKDDDIVESRYVEQHPDNEI
MIFCTGSQGEELAALNMLASGRHPWIQLKKTDSIIMSSNPIPGNYAAVERLLNELSKEEG
ISIYENSPTLKLHASGHATMQEIQLMLSLLRPKYLFPIHGEYKMFTSLKRIAKKCGFDPE
NVALHKNGQIVYLIDRELYYTKETIDAEPLFIEGKSVSPNVKRIMNTRQVLSEEGIFAIT
VVIDKASKQIKTLPKLKSSGCFYLKESHGLMTKIAYEIKTNANEYLAKNQNYSEHELKKI
IHESCRFYIWRNKHRNPLVVSNIREI






















© Fisunov Lab of Proteomics, 2016.